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ABC transporter C family member 3 (ABC transporter ABCC.3) (AtABCC3) (EC 3.6.3.44) (ATP-energized glutathione S-conjugate pump 3) (Glutathione S-conjugate-transporting ATPase 3) (Multidrug resistance-associated protein 3)

 AB3C_ARATH              Reviewed;        1514 AA.
Q9LK64; O24510; Q3EB73;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 130.
RecName: Full=ABC transporter C family member 3;
Short=ABC transporter ABCC.3;
Short=AtABCC3;
EC=3.6.3.44;
AltName: Full=ATP-energized glutathione S-conjugate pump 3;
AltName: Full=Glutathione S-conjugate-transporting ATPase 3;
AltName: Full=Multidrug resistance-associated protein 3;
Name=ABCC3; Synonyms=EST2, MRP3; OrderedLocusNames=At3g13080;
ORFNames=MJG19.3;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
STRAIN=cv. Columbia;
PubMed=9271206; DOI=10.1016/S0014-5793(97)00702-3;
Tommasini R., Vogt E., Schmid J., Fromentau M., Amrhein N.,
Martinoia E.;
"Differential expression of genes coding for ABC transporters after
treatment of Arabidopsis thaliana with xenobiotics.";
FEBS Lett. 411:206-210(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
INDUCTION.
PubMed=9671034; DOI=10.1007/s004380050779;
Sanchez-Fernandez R., Ardiles-Diaz W., Van Montagu M., Inze D.,
May M.J.;
"Cloning and expression analyses of the AtMRP4, a novel MRP-like gene
from Arabidopsis thaliana.";
Mol. Gen. Genet. 258:655-662(1998).
[5]
FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
SPECIFICITY.
PubMed=9681016; DOI=10.1046/j.1365-313X.1998.00076.x;
Tommasini R., Vogt E., Fromenteau M., Hoertensteiner S., Matile P.,
Amrhein N., Martinoia E.;
"An ABC-transporter of Arabidopsis thaliana has both glutathione-
conjugate and chlorophyll catabolite transport activity.";
Plant J. 13:773-780(1998).
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11346655; DOI=10.1074/jbc.M103104200;
Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
"The Arabidopsis thaliana ABC protein superfamily, a complete
inventory.";
J. Biol. Chem. 276:30231-30244(2001).
[7]
GENE FAMILY.
PubMed=11855639; DOI=10.1007/s004250100661;
Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
"Multifunctionality of plant ABC transporters -- more than just
detoxifiers.";
Planta 214:345-355(2002).
[8]
TISSUE SPECIFICITY.
PubMed=12430019; DOI=10.1007/s00425-002-0890-6;
Kolukisaoglu U.H., Bovet L., Klein M., Eggmann T., Geisler M.,
Wanke D., Martinoia E., Schulz B.;
"Family business: the multidrug-resistance related protein (MRP) ABC
transporter genes in Arabidopsis thaliana.";
Planta 216:107-119(2002).
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A.,
Rea P.A., Samuels L., Schulz B., Spalding E.J., Yazaki K.,
Theodoulou F.L.;
"Plant ABC proteins - a unified nomenclature and updated inventory.";
Trends Plant Sci. 13:151-159(2008).
-!- FUNCTION: Pump for glutathione S-conjugates. Mediates the
transport of glutathione conjugates such as chlorodinitrobenzene-
GS (DNB-GS), and of chlorophyll catabolites such as Bn-NCC-1.
Transports also heavy metals such as cadmium (Cd).
{ECO:0000269|PubMed:9681016}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + xenobiotic(In) = ADP + phosphate
+ xenobiotic(Out).
-!- ENZYME REGULATION: Glutathione-conjugate transport is inhibited by
decyl-glutathione and, to a lower extent, by GS-GS, but not by
GSH. All transports are inhibited by vanadate.
{ECO:0000269|PubMed:9681016}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=100 uM for DNB-GS (at pH 7.4 and 25 degrees Celsius)
{ECO:0000269|PubMed:9681016};
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-
ProRule:PRU00441}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00441}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9LK64-1; Sequence=Displayed;
Name=2;
IsoId=Q9LK64-2; Sequence=VSP_018099;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12430019,
ECO:0000269|PubMed:9681016}.
-!- INDUCTION: By 1-chloro-2,4-dinitrobenzene (CDNB), primisulfuron
(PS), aminotriazole, benoxacor, oxabetrinil and IRL 1803, and, to
a lower extent, by cloquintocet, fenchlorazol and fluorazol.
{ECO:0000269|PubMed:9271206, ECO:0000269|PubMed:9671034}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC49791.1; Type=Frameshift; Positions=1159, 1169, 1186, 1189, 1196; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U92650; AAC49791.1; ALT_FRAME; mRNA.
EMBL; AP000375; BAB01399.1; -; Genomic_DNA.
EMBL; CP002686; AEE75291.1; -; Genomic_DNA.
EMBL; CP002686; AEE75292.1; -; Genomic_DNA.
PIR; T52081; T52081.
RefSeq; NP_187915.1; NM_112147.3. [Q9LK64-1]
RefSeq; NP_850575.1; NM_180244.1. [Q9LK64-2]
UniGene; At.20479; -.
ProteinModelPortal; Q9LK64; -.
SMR; Q9LK64; -.
STRING; 3702.AT3G13080.1; -.
TCDB; 3.A.1.208.17; the atp-binding cassette (abc) superfamily.
PaxDb; Q9LK64; -.
PRIDE; Q9LK64; -.
EnsemblPlants; AT3G13080.1; AT3G13080.1; AT3G13080. [Q9LK64-1]
EnsemblPlants; AT3G13080.2; AT3G13080.2; AT3G13080. [Q9LK64-2]
GeneID; 820496; -.
Gramene; AT3G13080.1; AT3G13080.1; AT3G13080.
Gramene; AT3G13080.2; AT3G13080.2; AT3G13080.
KEGG; ath:AT3G13080; -.
Araport; AT3G13080; -.
TAIR; locus:2090029; AT3G13080.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
InParanoid; Q9LK64; -.
OMA; MRVVKYF; -.
OrthoDB; EOG0936009E; -.
PhylomeDB; Q9LK64; -.
BioCyc; ARA:AT3G13080-MONOMER; -.
PRO; PR:Q9LK64; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LK64; baseline and differential.
Genevisible; Q9LK64; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IDA:TAIR.
GO; GO:0010290; F:chlorophyll catabolite transmembrane transporter activity; IDA:TAIR.
GO; GO:0015431; F:glutathione S-conjugate-exporting ATPase activity; IDA:TAIR.
GO; GO:0008559; F:xenobiotic-transporting ATPase activity; IEA:UniProtKB-EC.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Hydrolase;
Membrane; Nucleotide-binding; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1514 ABC transporter C family member 3.
/FTId=PRO_0000226074.
TRANSMEM 35 55 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 83 103 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 116 136 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 153 173 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 183 203 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 325 345 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 364 386 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 439 459 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 463 483 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 551 571 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 940 960 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 987 1007 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 1077 1097 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 1181 1201 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 1205 1225 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
DOMAIN 325 606 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 640 863 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 950 1232 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1271 1503 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 675 682 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1303 1310 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
COMPBIAS 1507 1512 Poly-Ser.
VAR_SEQ 1347 1372 SIIPQDPTMFEGTMRSNLDPLEEYTD -> N (in
isoform 2). {ECO:0000305}.
/FTId=VSP_018099.
SEQUENCE 1514 AA; 168971 MW; 455575FCD3DA5115 CRC64;
MDFLGSTTGS GTLAMLFSFS ESILPLDSRS FLLKPLFLRW LSGFLHSVLL LVLFFSWVRK
KIRGDSGVTE SLKDRRDFGF KSALFCSLAL SLLNLVLMSL SGFYWYESGW LDNEQLVSSL
GFLLGMVSWG VLSICLHRCR DCEHKKAPFL LRLWLVFYLV VSCYSLVVDF VMYERRETVP
VHLLVFDIVA FIAAVFLGYV AVLKKDRSNS NGVLEEPLLN GGDSRVGGDD SVELNKTNGS
GEATPYSRAG ILSLLTFSWM SPLIDIGNKK TLDLEDVPQL HDTDSVVGLA PKFRSMLESP
DGGERSGVTT FKLIKALYFT AQWEILVTAF FAFIYTVASY VGPALIDTFV QYLNGRRQYN
HEGYVLVITF FAAKIVECLS QRHWFFRLQK VGIRMRSALV AMIYEKGLTL SCQSKQGRTS
GEIINFMTVD AERIGNFSWY MHDPWMVLLQ VGLALWILYR NLGLASIAAL VATIIVMLIN
FPFGRMQERF QEKLMEAKDS RMKSTSEILR NMRILKLQGW EMKFLSKIFD LRKSEEGWLK
KYVYNSAVIS FVFWGAPTLV SVSTFGACIL LGIPLESGKI LSALATFRIL QEPIYNLPDT
ISMIVQTKVS LDRLASYLCL DNLQPDIVER LPKGSSDVAV EVINSTLSWD VSSSNPTLKD
INFKVFPGMK VAVCGTVGSG KSSLLSSLLG EVPKVSGSLK VCGTKAYVAQ SPWIQSGKIE
DNILFGKPME RERYDKVLEA CSLSKDLEIL SFGDQTVIGE RGINLSGGQK QRIQIARALY
QDADIYLFDD PFSAVDAHTG SHLFKEVLLG LLCSKSVIYV THQVEFLPAA DLILVMKDGR
ISQAGKYNDI LNSGTDFMEL IGAHQEALAV VDSVDANSVS EKSALGQENV IVKDAIAVDE
KLESQDLKND KLESVEPQRQ IIQEEEREKG SVALDVYWKY ITLAYGGALV PFILLGQVLF
QLLQIGSNYW MAWATPVSED VQAPVKLSTL MIVYVALAFG SSLCILLRAT LLVTAGYKTA
TELFHKMHHC IFRSPMSFFD STPSGRIMSR ASTDQSAVDL ELPYQFGSVA ITVIQLIGII
GVMSQVSWLV FLVFIPVVAA SIWYQRYYIA AARELSRLVG VCKAPLIQHF SETISGATTI
RSFSQEFRFR SDNMRLSDGY SRPKFYTAGA MEWLCFRLDM LSSLTFVFSL VFLVSIPTGV
IDPSLAGLAV TYGLSLNTLQ AWLIWTLCNL ENKIISVERI LQYASVPSEP PLVIESNRPE
QSWPSRGEVE IRDLQVRYAP HMPLVLRGIT CTFKGGLRTG IVGRTGSGKS TLIQTLFRIV
EPSAGEIRID GVNILTIGLH DLRLRLSIIP QDPTMFEGTM RSNLDPLEEY TDDQIWEALD
KCQLGDEVRK KEQKLDSSVS ENGDNWSMGQ RQLVCLGRVL LKRSKILVLD EATASVDTAT
DNLIQKTLRE HFSDCTVITI AHRISSVIDS DMVLLLSNGI IEEYDTPVRL LEDKSSSFSK
LVAEYTSRSS SSFD


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